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Vitamin B12 Phosphate Conjugation and Its Effect on Binding to the Human B12 -Binding Proteins Intrinsic Factor and Haptocorrin

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Vitamin B12 Phosphate Conjugation and Its Effect on Binding to the Human B12 -Binding Proteins Intrinsic Factor and Haptocorrin. / Ó Proinsias, Keith; Ociepa, Michał; Pluta, Katarzyna; Chromiński, Mikołaj; Nexo, Ebba; Gryko, Dorota.

I: Chemistry: A European Journal, Bind 22, Nr. 24, 06.06.2016, s. 8282-9.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Ó Proinsias, K, Ociepa, M, Pluta, K, Chromiński, M, Nexo, E & Gryko, D 2016, 'Vitamin B12 Phosphate Conjugation and Its Effect on Binding to the Human B12 -Binding Proteins Intrinsic Factor and Haptocorrin', Chemistry: A European Journal, bind 22, nr. 24, s. 8282-9. https://doi.org/10.1002/chem.201504898

APA

Ó Proinsias, K., Ociepa, M., Pluta, K., Chromiński, M., Nexo, E., & Gryko, D. (2016). Vitamin B12 Phosphate Conjugation and Its Effect on Binding to the Human B12 -Binding Proteins Intrinsic Factor and Haptocorrin. Chemistry: A European Journal, 22(24), 8282-9. https://doi.org/10.1002/chem.201504898

CBE

MLA

Vancouver

Ó Proinsias K, Ociepa M, Pluta K, Chromiński M, Nexo E, Gryko D. Vitamin B12 Phosphate Conjugation and Its Effect on Binding to the Human B12 -Binding Proteins Intrinsic Factor and Haptocorrin. Chemistry: A European Journal. 2016 jun 6;22(24):8282-9. https://doi.org/10.1002/chem.201504898

Author

Ó Proinsias, Keith ; Ociepa, Michał ; Pluta, Katarzyna ; Chromiński, Mikołaj ; Nexo, Ebba ; Gryko, Dorota. / Vitamin B12 Phosphate Conjugation and Its Effect on Binding to the Human B12 -Binding Proteins Intrinsic Factor and Haptocorrin. I: Chemistry: A European Journal. 2016 ; Bind 22, Nr. 24. s. 8282-9.

Bibtex

@article{b84b214385cc4b7e99c8a50374f539f0,
title = "Vitamin B12 Phosphate Conjugation and Its Effect on Binding to the Human B12 -Binding Proteins Intrinsic Factor and Haptocorrin",
abstract = "The binding of vitamin B12 derivatives to human B12 transporter proteins is strongly influenced by the type and site of modification of the cobalamin original structure. We have prepared the first cobalamin derivative modified at the phosphate moiety. The reaction conditions were fully optimized and its limitations examined. The resulting derivatives, particularly those bearing terminal alkyne and azide groups, were isolated and used in copper-catalyzed alkyne-azide cycloaddition reactions (CuAAC). Their sensitivity towards light revealed their potential as photocleavable molecules. The binding abilities of selected derivatives were examined and compared with cyanocobalamin. The interaction of the alkylated derivatives with haptocorrin was less affected than the interaction with intrinsic factor. Furthermore, the configuration of the phosphate moiety was irrelevant to the binding process.",
keywords = "Journal Article, Click Chemistry, Glycoproteins, Phosphates, Substituent effects, Vitamins",
author = "{{\'O} Proinsias}, Keith and Micha{\l} Ociepa and Katarzyna Pluta and Miko{\l}aj Chromi{\'n}ski and Ebba Nexo and Dorota Gryko",
note = "{\textcopyright} 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",
year = "2016",
month = jun,
day = "6",
doi = "10.1002/chem.201504898",
language = "English",
volume = "22",
pages = "8282--9",
journal = "Chemistry: A European Journal",
issn = "0947-6539",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "24",

}

RIS

TY - JOUR

T1 - Vitamin B12 Phosphate Conjugation and Its Effect on Binding to the Human B12 -Binding Proteins Intrinsic Factor and Haptocorrin

AU - Ó Proinsias, Keith

AU - Ociepa, Michał

AU - Pluta, Katarzyna

AU - Chromiński, Mikołaj

AU - Nexo, Ebba

AU - Gryko, Dorota

N1 - © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

PY - 2016/6/6

Y1 - 2016/6/6

N2 - The binding of vitamin B12 derivatives to human B12 transporter proteins is strongly influenced by the type and site of modification of the cobalamin original structure. We have prepared the first cobalamin derivative modified at the phosphate moiety. The reaction conditions were fully optimized and its limitations examined. The resulting derivatives, particularly those bearing terminal alkyne and azide groups, were isolated and used in copper-catalyzed alkyne-azide cycloaddition reactions (CuAAC). Their sensitivity towards light revealed their potential as photocleavable molecules. The binding abilities of selected derivatives were examined and compared with cyanocobalamin. The interaction of the alkylated derivatives with haptocorrin was less affected than the interaction with intrinsic factor. Furthermore, the configuration of the phosphate moiety was irrelevant to the binding process.

AB - The binding of vitamin B12 derivatives to human B12 transporter proteins is strongly influenced by the type and site of modification of the cobalamin original structure. We have prepared the first cobalamin derivative modified at the phosphate moiety. The reaction conditions were fully optimized and its limitations examined. The resulting derivatives, particularly those bearing terminal alkyne and azide groups, were isolated and used in copper-catalyzed alkyne-azide cycloaddition reactions (CuAAC). Their sensitivity towards light revealed their potential as photocleavable molecules. The binding abilities of selected derivatives were examined and compared with cyanocobalamin. The interaction of the alkylated derivatives with haptocorrin was less affected than the interaction with intrinsic factor. Furthermore, the configuration of the phosphate moiety was irrelevant to the binding process.

KW - Journal Article

KW - Click Chemistry

KW - Glycoproteins

KW - Phosphates

KW - Substituent effects

KW - Vitamins

U2 - 10.1002/chem.201504898

DO - 10.1002/chem.201504898

M3 - Journal article

C2 - 27120016

VL - 22

SP - 8282

EP - 8289

JO - Chemistry: A European Journal

JF - Chemistry: A European Journal

SN - 0947-6539

IS - 24

ER -